ID A0A093P981_PYGAD Unreviewed; 822 AA.
AC A0A093P981;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Enhancer of filamentation 1 {ECO:0000313|EMBL:KFW68817.1};
DE Flags: Fragment;
GN ORFNames=AS28_04289 {ECO:0000313|EMBL:KFW68817.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW68817.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW68817.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW68817.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}.
CC -!- SIMILARITY: Belongs to the CAS family. {ECO:0000256|ARBA:ARBA00007848}.
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DR EMBL; KL225213; KFW68817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093P981; -.
DR STRING; 9238.A0A093P981; -.
DR Proteomes; UP000054081; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd11570; FAT-like_NEDD9_C; 1.
DR CDD; cd11550; Serine_rich_NEDD9; 1.
DR CDD; cd12002; SH3_NEDD9; 1.
DR Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 1.
DR Gene3D; 1.20.120.830; Serine-rich domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR021901; CAS_C.
DR InterPro; IPR037362; CAS_fam.
DR InterPro; IPR035746; NEDD9_SH3.
DR InterPro; IPR014928; Serine_rich_dom.
DR InterPro; IPR038319; Serine_rich_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10654; CAS SCAFFOLDING PROTEIN; 1.
DR PANTHER; PTHR10654:SF20; ENHANCER OF FILAMENTATION 1; 1.
DR Pfam; PF12026; CAS_C; 1.
DR Pfam; PF08824; Serine_rich; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000054081};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..62
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 360..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 432..493
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW68817.1"
FT NON_TER 822
FT /evidence="ECO:0000313|EMBL:KFW68817.1"
SQ SEQUENCE 822 AA; 91910 MW; A5678A54D539C623 CRC64;
QNLMARALYD NVPECAEELA FRKGDILTVI EQNTEGLEGW WLCSLHGRQG IVPGNRVKLL
IGPVVQDSPG QDMSNSGLMH QSFNQQKIYQ VPSSHASARD PVYQVPPSHL NQGIYQIPTG
HGLVGQDIYQ VPPSMQRCID GPALTNKVIT PVRSGQGYVY EFPSKYQKDT YDIPPVRPLQ
GIYDIPPTSV KGPALPVPMG EAKALGVYDI PPAKGVYATP PSACRNDTGP RENLQGFSSP
VGHSVRPEGV YDIPPPITKA TEKELNKFSP ESLLLPDGVP QKQNVYDIPM NHQNHFLGQQ
IAAQKDVYDT PRGIPFPGQQ TGLSESLIPE GREGVYDVPP PVLQDTKGLQ DVTDGINRLS
FSSTGSTRSN MSTSSTTSKD SSFSASTAQD KRLILDPDTA IERLYRLQQM VETAVNNLMA
FVTADWRSYA YMEKHINEIH TAVDKVEQLL LEYLQFAKGS AANASCLSEF SLLNKMRREV
QRLEDSHQIL TQTSHDLNSY NWSLNVLAVN RLQNKCDDLD RFVMVARTVP DDAKQLTTTI
SVNAEVLFKQ ALSSSRFKNI PENIMNTPDY VYDNPHMQHH GEKAQNHCSS LPPLLSKGQH
PHNTTSDSSE KSWMDDYDYV HLQGKEEFER QQKELLEKEN IIKQSKMELE HHQINQFQRL
EQEITKPVEN DISKWKPPQA LQTANSTAAS HDSQLLLFYS DQCETHFNSL LNAIDAFFSC
VNASQPPRIF VAHSKFVILS AHKLVFIGDM LTRQVTTQDI CNKVMNSSNQ LCELLKSVVL
ATKMAALHYP NTAALQKMVD RVTELSHHAQ LFKLSLVQMA SL
//